Structure of Thermolysin Cleaved Microcin J25:  Extreme Stability of a Two-Chain Antimicrobial Peptide Devoid of Covalent Links†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (16) ◽  
pp. 4696-4702 ◽  
Author(s):  
K. Johan Rosengren ◽  
Alain Blond ◽  
Carlos Afonso ◽  
Jean-Claude Tabet ◽  
Sylvie Rebuffat ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Microcin J25 ◽  
Extreme Stability

Solution structure of microcin J25, the single macrocyclic antimicrobial peptide from Escherichia coli

2001 ◽  
Vol 268 (7) ◽  
pp. 2124-2133 ◽  
Author(s):  
Alain Blond ◽  
Michel Cheminant ◽  
Isabelle Ségalas-Milazzo ◽  
Jean Péduzzi ◽  
Michel Barthélémy ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antimicrobial Peptide ◽  
Solution Structure ◽  
Microcin J25

scholarly journals Effect of Antimicrobial Peptide Microcin J25 on Growth Performance, Immune Regulation, and Intestinal Microbiota in Broiler Chickens Challenged with Escherichia coli and Salmonella

Animals ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 345 ◽  
Author(s):  
Gang Wang ◽  
Qinglong Song ◽  
Shuo Huang ◽  
Yuming Wang ◽  
Shuang Cai ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Growth Performance ◽  
Intestinal Microbiota ◽  
Immune Regulation ◽  
Broiler Chickens ◽  
Body Weight Gain ◽  
The Body ◽  
Villus Height ◽  
Microcin J25 ◽  
Challenge Group

The purpose of this study was to investigate the effects of antimicrobial peptide microcin J25 (MccJ25) on growth performance, immune regulation, and intestinal microbiota in broilers. A total of 3120 one-day-old male Arbor Acres (AA) broilers were randomly allocated to five groups (12 replicates, 52 chickens per replicate). The treatments were control, challenge (0 mg/kg MccJ25), different dosages of antimicrobial peptide (AMP) (0.5 and 1mg/kg MccJ25), and antibiotic groups (20 mg/kg colistin sulfate). The MccJ25 groups increased the body weight gain (starter and overall) that was reduced in the challenge group. The overall (day 1 to day 42) feed-to-gain ratio (G:F) was significantly decreased in AMP groups compared with the challenge group. Birds fed AMP had a decreased population of total anaerobic bacteria (day 21 and day 42) and E. coli (day 21 and day 42) in feces, as well as a lower Salmonella infection rate (day 21 and day 42) compared with birds in the challenge group. The villus height of the duodenum, jejunum, and ileum, as well as the villus height/crypt depth of the duodenum and jejunum were greater in AMP groups than birds in the challenge group. Moreover, MccJ25 linearly improved the villus height of the duodenum and jejunum. The addition of MccJ25 decreased the concentration of TNF-α, IL-1β, and IL-6 compared with challenge group. At d 21, MccJ25 linearly reduced the level of IL-6. In conclusion, dietary supplemented MccJ25 effectively improved performance, systematic inflammation, and improved fecal microbiota composition of the broilers.

Penetration and interactions of the antimicrobial peptide, microcin J25, into uncharged phospholipid monolayers

2005 ◽  
Vol 285 (1) ◽  
pp. 118-124 ◽  
Author(s):  
Augusto Bellomio ◽  
Rafael G. Oliveira ◽  
Bruno Maggio ◽  
Roberto D. Morero
Keyword(s):  
Antimicrobial Peptide ◽  
Phospholipid Monolayers ◽  
Microcin J25

scholarly journals The iron–siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11–Pro16 β-hairpin region in the recognition mechanism

2005 ◽  
Vol 389 (3) ◽  
pp. 869-876 ◽  
Author(s):  
Delphine Destoumieux-Garzón ◽  
Sophie Duquesne ◽  
Jean Peduzzi ◽  
Christophe Goulard ◽  
Michel Desmadril ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Size Exclusion ◽  
Receptor Interaction ◽  
Titration Calorimetry ◽  
Scanning Calorimetry ◽  
Recognition Mechanism ◽  
Microcin J25

The role of the outer-membrane iron transporter FhuA as a potential receptor for the antimicrobial peptide MccJ25 (microcin J25) was studied through a series of in vivo and in vitro experiments. The requirement for both FhuA and the inner-membrane TonB–ExbB–ExbD complex was demonstrated by antibacterial assays using complementation of an fhuA− strain and by using isogenic strains mutated in genes encoding the protein complex respectively. In addition, MccJ25 was shown to block phage T5 infection of Escherichia coli, in vivo, by inhibiting phage adhesion, which suggested that MccJ25 prevents the interaction between the phage and its receptor FhuA. This in vivo activity was confirmed in vitro, as MccJ25 inhibited phage T5 DNA ejection triggered by purified FhuA. Direct interaction of MccJ25 with FhuA was demonstrated for the first time by size-exclusion chromatography and isothermal titration calorimetry. MccJ25 bound to FhuA with a 2:1 stoichiometry and a Kd of 1.2 μM. Taken together, our results demonstrate that FhuA is the receptor for MccJ25 and that the ligand–receptor interaction may occur in the absence of other components of the bacterial membrane. Finally, both differential scanning calorimetry and antimicrobial assays showed that MccJ25 binding involves external loops of FhuA. Unlike native MccJ25, a thermolysin-cleaved MccJ25 variant was unable to bind to FhuA and failed to prevent phage T5 infection of E. coli. Therefore the Val11–Pro16 β-hairpin region of MccJ25, which is disrupted upon cleavage by thermolysin, is required for microcin recognition.

Engineered gene clusters for the production of the antimicrobial peptide microcin J25

2010 ◽  
Vol 71 (2) ◽  
pp. 200-206 ◽  
Author(s):  
Si Jia Pan ◽  
Wai Ling Cheung ◽  
A. James Link
Keyword(s):  
Antimicrobial Peptide ◽  
Gene Clusters ◽  
Microcin J25

Antimitochondrial activity displayed by the antimicrobial peptide microcin J25

2004 ◽  
Vol 317 (3) ◽  
pp. 882-886 ◽  
Author(s):  
Marı́a V. Niklison Chirou ◽  
Carlos J. Minahk ◽  
Roberto D. Morero
Keyword(s):  
Antimicrobial Peptide ◽  
Microcin J25
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